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The salt‐soluble proteins of barley. II. —the detailed composition of saline extracts of barley‐fractionation by precipitation with ammonium sulphate
Author(s) -
Pool A. A.,
Shooter E. M.
Publication year - 1955
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.2740060909
Subject(s) - fractionation , ammonium , salt (chemistry) , chemistry , globulin , composition (language) , chromatography , electrophoresis , hordeum vulgare , precipitation , albumin , ammonium sulfate , biochemistry , botany , poaceae , biology , organic chemistry , linguistics , philosophy , physics , meteorology , immunology
Approximately 10% of the total nitrogen content of barley grain may be extracted from ground barley (Spratt‐Archer) with saline solutions under conditions chosen to minimize proteinase activity. Electrophoretic analysis of arbitrary fractions produced from these extracts by ammonium sulphate show that they contain many non‐dialysable compounds. At least two more major components are revealed by the electrophoretic analysis than may be accounted for by Quensel's four globulins and the barley albumin of Danielsson and Sandegren. Of the numerous minor components, one contains nucleic acid whilst a second probably belongs to the general class of plant proteinases. The non‐protein material is derived mainly from the barley gums and is chiefly precipitated in the fraction precipitated between 0.7‐1.0 saturation with ammonium sulphate.